ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry A4XKT2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PYRC_CALS8
Primary accession number A4XKT2
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on May 29, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 14)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: Csac_1932
From
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [TaxID: 351627] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.;
"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000679; ABP67517.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001180708.1; -.
3D structure databases
ModBase A4XKT2.
Ontologies
GO
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from HAMAP).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00220; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00857; pyrC_multi; 1.
PROSITE PS00482; DIHYDROOROTASE_1; FALSE_NEG.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS A4XKT2.
Genome annotation databases
GeneID 5089294; -.
GenomeReviews CP000679_GR; Csac_1932.
KEGG csc:Csac_1932; -.
CMR A4XKT2; Csac_1932.
Other
ProtoNet A4XKT2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   430  430     Dihydroorotase. PRO_0000325590
METAL   61    61        Zinc 1 (By similarity). 
METAL   63    63        Zinc 1 (By similarity). 
METAL   143   143        Zinc 1; via carbamate group (By similarity). 
METAL   143   143        Zinc 2; via carbamate group (By similarity). 
METAL   180   180        Zinc 2 (By similarity). 
METAL   233   233        Zinc 2 (By similarity). 
METAL   306   306        Zinc 1 (By similarity). 
MOD_RES   143   143        N6-carboxylysine (By similarity). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 47394 Da [This is the MW of the unprocessed precursor] CRC64: 75C5C16A7ED4318E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MILIKNAQII NSLHDKVEKA DILIVDDKIK KIGKDIEENP EKMTIIDASG KVVMPSFTDI 

        70         80         90        100        110        120 
HCHLREPGFE YKEDIKSGSR SAAAGGFTTI CCMPNTNPPV DNRAMVAYIK YRAREVSPIE 

       130        140        150        160        170        180 
VLPVGAITKG LLGEELAEIG FMKEEGAIAI SDDGKCVMNA NLMKNALLYS RDFSIPVISH 

       190        200        210        220        230        240 
CEDTNLSEGG QINLGYVSTI TGLRGIPREA ESVIIARDIL LAKETKSHLH ITHVSTKESV 

       250        260        270        280        290        300 
RLIKMAKEWG VNVTADTCPH YISLTEEEVL GFNTNAKVNP PLRTQEDVEA LIEGLKEGVI 

       310        320        330        340        350        360 
DCISTDHAPH HKDEKNVEFN LAASGTIGFE TAFSVLFTYL VEKNGFDIGK IVELLNHNPR 

       370        380        390        400        410        420 
KIIGLSPNVL KEGEKANLVI VDLKKKWEVK EENIVSKSKN SVFLGKLLTS YVETVIYNGK 

       430 
ILKKDGVLNC
A4XKT2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!